+Open data
-Basic information
Entry | Database: PDB / ID: 5xd6 | ||||||
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Title | CARK1 phosphorylates ABA receptors | ||||||
Components | Protein kinase superfamily protein | ||||||
Keywords | TRANSFERASE / Kinase / Phosphorylation / ABA signaling | ||||||
Function / homology | Function and homology information positive regulation of response to water deprivation / positive regulation of abscisic acid-activated signaling pathway / abscisic acid-activated signaling pathway / non-specific serine/threonine protein kinase / protein phosphorylation / protein serine/threonine kinase activity / magnesium ion binding / ATP binding / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Arabidopsis thaliana (thale cress) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.898 Å | ||||||
Authors | Zhang, L. / Lou, Z. | ||||||
Citation | Journal: To Be Published Title: CARK1 phosphorylates ABA receptors Authors: Zhang, L. / Lou, Z. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5xd6.cif.gz | 132.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5xd6.ent.gz | 100.9 KB | Display | PDB format |
PDBx/mmJSON format | 5xd6.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xd/5xd6 ftp://data.pdbj.org/pub/pdb/validation_reports/xd/5xd6 | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 33366.164 Da / Num. of mol.: 2 / Fragment: UNP residues 50-350 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: At3g17410, AXX17_At3g18370 / Production host: Escherichia coli K-12 (bacteria) / References: UniProt: Q9LUT0 #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.59 Å3/Da / Density % sol: 52.55 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop Details: 0.1M ammonium acetate, 0.1M Bis-Tris (pH 5.5), 17%(w/v) PEG 10,000 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 1 Å |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: May 23, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.898→50 Å / Num. obs: 53775 / % possible obs: 98.4 % / Redundancy: 3.9 % / CC1/2: 0.847 / Rmerge(I) obs: 0.055 / Net I/av σ(I): 21.5 / Net I/σ(I): 15 |
Reflection shell | Resolution: 1.9→1.93 Å / Redundancy: 3.1 % / Rmerge(I) obs: 0.596 / Mean I/σ(I) obs: 1.94 / Num. unique obs: 2522 / % possible all: 93.2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.898→29.755 Å / SU ML: 0.24 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 29.74
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||
Displacement parameters | Biso max: 499.69 Å2 / Biso mean: 36.8924 Å2 / Biso min: 16.57 Å2 | ||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 1.898→29.755 Å
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